Symbol FCER1A Entrez 2205 OMIM 147140 | Alt. symbols FcεRIα, FCE1A HUGO 3609 RefSeq NM_002001 | |
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The high-affinity IgE receptor, also known as FcεRI, or Fc epsilon RI, is the high-affinity receptor for the Fc region of immunoglobulin E (IgE), an antibody isotype involved in the allergy disorder and parasites immunity. FcεRI is a tetrameric receptor complex that binds Fc portion of the ε heavy chain of IgE. It consists of one alpha (FcεRIα - antibody binding site), one beta (FcεRIβ - which amplifies the downstream signal), and two gamma chains (FcεRIγ - the site where the downstream signal initiates) connected by two disulfide bridges. It is constitutively expressed on mast cells and basophils and is inducible in eosinophils.
Contents
Tissue distribution
FcεRI is found on epidermal Langerhans cells, eosinophils, mast cells, and basophils. As a result of its cellular distribution, this receptor plays a major role in controlling allergic responses. FcεRI is also expressed on antigen-presenting cells, and controls the production of important immune mediators (cytokines, interleukins, leukotrienes, and prostaglandins) that promote inflammation. The most famous mediator is histamine, which results in the five symptoms of inflammation: heat, swelling, pain, redness and itchiness.
Mechanism of action
Crosslinking of the FcεRI via IgE-antigen complexes leads to degranulation of mast cells or basophils and release of inflammatory mediators. Under laboratory conditions, degranulation of isolated basophils can also be induced with antibodies to the FcεRIα, which crosslink the receptor. Such crosslinking and potentially pathogenic autoantibodies to the FcεRIα have been isolated from human cord blood, which suggest that they occur naturally and are present already at birth. However, their epitope on FcεRIα was masked by IgE, and the affinity of the corresponding autoantibodies found in healthy adults appeared lowered.